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Endocytosis of fibrinogen into megakaryocyte and platelet alpha- granules
is mediated by alpha IIb beta 3 (glycoprotein IIb-IIIa) [published erratum
appears in Blood 1993 Nov 1;82(9):2936]
P Handagama, RM Scarborough, MA Shuman and DF Bainton
Department of Pathology, University of California, San Francisco 94143-
0506.
Recently, we showed that platelet alpha-granule fibrinogen is derived
entirely from endocytic uptake and not from megakaryocyte synthesis, as
previously thought. In this present report, we identify the receptor that
mediates endocytosis. We have found that barbourin, a unique disintegrin
that is a specific antagonist of alpha IIb beta 3, inhibits the endocytic
uptake of fibrinogen into alpha-granules. Continuous intravenous infusion
of barbourin (200 micrograms/h) into guinea pigs blocked collagen-induced
platelet aggregation as well as endocytosis of biotinylated fibrinogen into
megakaryocytes; however, endocytosis of biotinylated albumin by
megakaryocytes was not affected. Thus, we have shown that endocytosis of
fibrinogen into megakaryocyte and platelet alpha-granules is
receptor-mediated, and that alpha IIb beta 3 is the primary receptor.
Volume 82,
Issue 1,
pp. 135-138,
07/01/1993
Copyright © 1993 by The American Society of Hematology
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